1bbw
From Proteopedia
(New page: 200px<br /><applet load="1bbw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bbw, resolution 2.7Å" /> '''LYSYL-TRNA SYNTHETASE...) |
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| - | [[Image:1bbw.jpg|left|200px]]<br /><applet load="1bbw" size=" | + | [[Image:1bbw.jpg|left|200px]]<br /><applet load="1bbw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bbw, resolution 2.7Å" /> | caption="1bbw, resolution 2.7Å" /> | ||
'''LYSYL-TRNA SYNTHETASE (LYSS)'''<br /> | '''LYSYL-TRNA SYNTHETASE (LYSS)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA | + | Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate. A comparison between the unliganded and lysine-bound structures reveals major conformational changes upon lysine binding. The lysine substrate is involved in a network of hydrogen bonds. Two of these interactions, one between the alpha-amino group and the carbonyl oxygen of Gly 216 and the other between the carboxylate group and the side chain of Arg 262, trigger a subtle and complicated reorganization of the active site, involving the ordering of two loops (residues 215-217 and 444-455), a change in conformation of residues 393-409, and a rotation of a 4-helix bundle domain (located between motif 2 and 3) by 10 degrees. The result of these changes is a closing up of the active site upon lysine binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1BBW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Lysine--tRNA_ligase Lysine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.6 6.1.1.6] Full crystallographic information is available from [http:// | + | 1BBW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Lysine--tRNA_ligase Lysine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.6 6.1.1.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein biosynthesis]] | [[Category: protein biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:37 2008'' |
Revision as of 09:53, 21 February 2008
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LYSYL-TRNA SYNTHETASE (LYSS)
Overview
Lysyl-tRNA synthetase is a member of the class II aminoacyl-tRNA synthetases and catalyses the specific aminoacylation of tRNA(Lys). The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate. A comparison between the unliganded and lysine-bound structures reveals major conformational changes upon lysine binding. The lysine substrate is involved in a network of hydrogen bonds. Two of these interactions, one between the alpha-amino group and the carbonyl oxygen of Gly 216 and the other between the carboxylate group and the side chain of Arg 262, trigger a subtle and complicated reorganization of the active site, involving the ordering of two loops (residues 215-217 and 444-455), a change in conformation of residues 393-409, and a rotation of a 4-helix bundle domain (located between motif 2 and 3) by 10 degrees. The result of these changes is a closing up of the active site upon lysine binding.
About this Structure
1BBW is a Single protein structure of sequence from Escherichia coli. Active as Lysine--tRNA ligase, with EC number 6.1.1.6 Full crystallographic information is available from OCA.
Reference
Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding., Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P, Biochemistry. 2000 Oct 24;39(42):12853-61. PMID:11041850
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